Safety evaluation of the food enzyme α‐amylase from the genetically modified Bacillus licheniformis strain CCTCC M 2023118

TL;DR

This study evaluates the safety of a food enzyme produced from a genetically modified bacterium, finding potential risks related to allergens and a contaminant called citrinin.

Contribution

The study provides a safety assessment of a genetically modified α-amylase enzyme used in food manufacturing, highlighting potential allergenic and toxicological concerns.

Findings

The production strain contains an antimicrobial resistance gene, but the enzyme itself does not pose a risk due to absence of viable cells and DNA.

Citrinin contamination in the enzyme raises concerns about genotoxicity and carcinogenicity.

Potential allergenic risk exists due to sequence homology with respiratory allergens, though the likelihood is considered low.

Abstract

The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain CCTCC M 2023118 by Sunson Industry Group Co., Ltd. The production strain of the food enzyme contains multiple copies of a known antimicrobial resistance gene. Consequently, it does not fulfil the requirements for the qualified presumption of safety approach to safety assessment. However, considering the absence of viable cells and DNA from the production organism in the food enzyme, this is not considered to be a risk. No concerns were identified from the food enzyme manufacturing process. Citrinin was detected in all food enzyme preparation batches at a concentration exceeding 405 μg/kg. The food enzyme is intended to be used in six food manufacturing processes. Since residual amounts of food enzyme–total organic solids (TOS) are removed in two processes, dietary exposure was calculated for the remaining four food manufacturing processes. It was estimated to be up to 5.166 mg TOS/kg body weight per day in European populations. A search for the homology of the amino acid sequence of the α‐amylase to known allergens was made and two matches with respiratory allergens were found. The Panel considered that a risk of allergic reactions upon dietary exposure to the food enzyme cannot be excluded, but that the likelihood is low. Based on the data provided on the presence of citrinin in the food enzyme preparation, the Panel could not exclude genotoxicity and carcinogenicity concerns for the food enzyme.

Tables

TABLE 1. Composition of the food enzyme preparation.

Parameters	Unit	Batches
		1	2	3
α‐Amylase activity	U/g a	14,900	14,800	14,800
Protein	%	4.3	4.3	4.3
Ash	%	11.8	11.5	10.9
Water	%	40.4	40.4	40.2
Excipient ■■■■■	%	29.8	29.8	29.9
Total organic solids (TOS) b	%	18.0	18.3	19.0
Activity/TOS ratio	U/mg TOS	82.8	80.9	77.9

TABLE 2. Intended uses and recommended use levels of the food enzyme as provided by the applicant. 50

Food manufacturing process a	Raw material (RM)	Recommended use level (mg TOS/kg RM) b
Processing of cereals and other grains
Production of baked products	Flour	97–193
Production of cereal based products other than baked	Flour	290–386
Production of brewed products	Cereals	193–386
Production of glucose syrups and other starch hydrolysates	Starch based material	290–386
Production of distilled alcohol	Starch based material	193–386
Processing of plant‐ and fungal‐derived products
Production of plant‐based analogues of milk and milk products	Raw plant material	48–97

TABLE 3. Summary of the estimated dietary exposure to food enzyme–TOS in six population groups.

Population group	Estimated exposure (mg TOS/kg body weight per day)
	Infants	Toddlers	Children	Adolescents	Adults	The elderly
Age range	3–11 months	12–35 months	3–9 years	10–17 years	18–64 years	≥ 65 years
Min–max mean (number of surveys)	0.375–1.698 (12)	0.990–2.160 (15)	0.507–1.490 (19)	0.155–1.061 (21)	0.317–0.810 (22)	0.283–0.631 (23)
Min–max 95th percentile (number of surveys)	1.100–5.166 (11)	2.426–4.246 (14)	1.213–2.991 (19)	0.407–2.006 (20)	0.734–2.387 (22)	0.617–1.434 (22)

TABLE 4. Qualitative evaluation of the influence of uncertainties on the dietary exposure estimate.

Sources of uncertainties	Direction of impact
Model input data
Consumption data: different methodologies/representativeness/underreporting/misreporting/no portion size standard	+/−
Use of data from food consumption surveys of a few days to estimate long‐term (chronic) exposure for high percentiles (95th percentile)	+
Possible national differences in categorisation and classification of food	+/−
Model assumptions and factors
Selection of broad FoodEx categories for the exposure assessment	+
Exposure to food enzyme–TOS always calculated based on the recommended maximum use level	+
Use of recipe fractions to disaggregate FoodEx categories	+/−
Use of technical factors in the exposure model	+/−
Exclusion of two processes from the exposure estimation: – production of distilled alcohol – production of glucose syrups and other starch hydrolysates	−

Full text

INTRODUCTION

1

Article 3 of the Regulation (EC) No 1332/20081 provides definition for ‘food enzyme’ and ‘food enzyme preparation’.

‘Food enzyme’ means a product obtained from plants, animals or microorganisms or products thereof including a product obtained by a fermentation process using microorganisms: (i) containing one or more enzymes capable of catalysing a specific biochemical reaction; and (ii) added to food for a technological purpose at any stage of the manufacturing, processing, preparation, treatment, packaging, transport or storage of foods.

‘Food enzyme preparation’ means a formulation consisting of one or more food enzymes in which substances such as food additives and/or other food ingredients are incorporated to facilitate their storage, sale, standardisation, dilution or dissolution.

Before January 2009, food enzymes other than those used as food additives were not regulated or were regulated as processing aids under the legislation of the Member States. On 20 January 2009, Regulation (EC) No 1332/2008 on food enzymes came into force. This Regulation applies to enzymes that are added to food to perform a technological function in the manufacture, processing, preparation, treatment, packaging, transport or storage of such food, including enzymes used as processing aids. Regulation (EC) No 1331/20082 established the European Union (EU) procedures for the safety assessment and the authorisation procedure of food additives, food enzymes and food flavourings. The use of a food enzyme shall be authorised only if it is demonstrated that:

• it does not pose a safety concern to the health of the consumer at the level of use proposed;
• there is a reasonable technological need;
• its use does not mislead the consumer.

All food enzymes currently on the EU market and intended to remain on that market, as well as all new food enzymes, shall be subjected to a safety evaluation by the European Food Safety Authority (EFSA) and approval via an EU Community list.

Background and Terms of Reference as provided by the requestor

1.1

Background as provided by the European Commission

1.1.1

Only food enzymes included in the Union list may be placed on the market as such and used in foods, in accordance with the specifications and conditions of use provided for in Article 7(2) of Regulation (EC) No 1332/2008 on food enzymes.

On 10 July 2024, a new application was introduced by the applicant “Sunson Industry Group Co., Ltd.” for the authorisation of the food enzyme Alpha‐amylase from a genetically modified Bacillus licheniformis (strain M 2023118).

Terms of Reference

1.1.2

The European Commission requests the European Food Safety Authority to carry out the safety assessment and the assessment of possible confidentiality requests of the following food enzyme: Alpha‐amylase from a genetically modified Bacillus licheniformis (strain M 2023118) in accordance with Regulation (EC) No 1331/2008 establishing a common authorisation procedure for food additives, food enzymes and food flavourings.3

Interpretation of the Terms of Reference

1.2

The present scientific opinion addresses the European Commission's request to carry out the safety assessment of the food enzyme α‐amylase from Bacillus licheniformis strain M 2023118. The applicant refers to the production as B. licheniformis CCTCC M 2023118; therefore, this name will be used through the opinion.

DATA AND METHODOLOGIES

2

Data

2.1

The applicant has submitted a dossier in support of the application for authorisation of the food enzyme α‐amylase from Bacillus licheniformis CCTCC M 2023118.

Additional information, requested from the applicant during the assessment process on 12 February 2025, were received on 25 March 2025 (see ‘Section 5’).

Methodologies

2.2

The assessment was conducted in line with the principles described in the EFSA ‘Guidance on transparency in the scientific aspects of risk assessment’ (EFSA, 2009) and following the relevant guidance documents of the EFSA Scientific Committee.

The ‘Scientific Guidance for the submission of dossiers on food enzymes’ (EFSA CEP Panel, 2021) and the ‘Food manufacturing processes and technical data used in the exposure assessment of food enzymes’ (EFSA CEP Panel, 2023) have been followed for the evaluation.

Public consultation

2.3

According to Article 32c(2) of Regulation (EC) No 178/20024 and to the Decision of EFSA's Executive Director laying down the practical arrangements on pre‐submission phase and public consultations, EFSA carried out a public consultation on the non‐confidential version of the technical dossier from 23 May to 13 June 2025.5 No comments were received.

ASSESSMENT

3

IUBMB nomenclatureα‐AmylaseSystematic name4‐α‐d‐glucan glucanohydrolaseSynonymsGlycogenaseIUBMB NoEC 3.2.1.1CAS No9000‐90‐2EINECS No232‐565‐6

α‐Amylases catalyse the hydrolysis of 1,4‐α‐glucosidic linkages in starch (amylose and amylopectin), glycogen and related polysaccharides and oligosaccharides, resulting in the generation of soluble dextrins and other oligosaccharides.

The food enzyme under assessment is intended to be used in six food manufacturing processes as defined in the EFSA guidance (EFSA CEP Panel, 2023): processing of cereals and other grains for the production of (1) baked products, (2) cereal‐based products other than baked, (3) brewed products, (4) glucose syrups and other starch hydrolysates and (5) distilled alcohol; (6) processing of plant‐ and fungal‐derived products for the production of plant‐based analogues of milk and milk products.

Source of the food enzyme

3.1

The enzyme is produced with the genetically modified Bacillus licheniformis strain CCTCC M 2023118 ■■■■■, which is deposited at the China Centre for Type Culture Collection (CCTCC, China) with deposition number M 2023118.6 The production strain was identified as B. licheniformis based on the whole genome sequencing (WGS) analysis ■■■■■.7

The species B. licheniformis is included in the list of organisms for which the qualified presumption of safety (QPS) may be applied, provided that the absence of acquired antimicrobial resistance (AMR) genes and toxigenic activity are verified for the specific strain used, and the genetic modifications do not raise concerns (EFSA, 2007; EFSA BIOHAZ Panel, 2022).8 A cytotoxicity test made with culture supernatant indicated that the production strain B. licheniformis CCTCC M 2023118 did not induce cell damage to Vero cells using the lactate dehydrogenase assay (LDH).9 The WGS data from the production strain was searched for AMR genes using two regularly maintained databases. No genes of concern were identified with thresholds above 80% of identity and 70% of coverage.10 ^,^ 11 However, the applicant reported that ■■■■■.12 Therefore, the production strain does not meet the requirements to qualify for the QPS approach.

Characteristics of the parental microorganisms

3.1.1

The parental strain ■■■■■13 ■■■■■.14

Characteristics of introduced sequences

3.1.2

The sequence encoding the α‐amylase ■■■■■15 ■■■■■16 ■■■■■.17

Description of the genetic modification

3.1.3

The purpose of the genetic modification was to enable the production strain ■■■■■ the α‐amylase ■■■■■18 ^,^ 19 ■■■■■20 ^,^ 21

Safety aspects of the genetic modification

3.1.4

The technical dossier contains all necessary information on the parental microorganism and the genetic modification process.

The production strain B. licheniformis CCTCC M 2023118, differs from the recipient strain ■■■■■.22 In addition, the production strain was found unable to sporulate.23 ^,^ 24

The presence of ■■■■■ in the production strain conferring antimicrobial resistance is considered a hazard.

Production of the food enzyme

3.2

The food enzyme is manufactured according to the Food Hygiene Regulation (EC) No 852/2004,25 with food safety procedures based on Hazard Analysis and Critical Control Points, and in accordance with Good Manufacturing Practice.26

The production strain is grown as a pure culture using a typical industrial medium in a submerged, fed‐batch fermentation system with conventional process controls in place. After completion of the fermentation, the solid biomass is removed from the fermentation broth by filtration. The filtrate containing the enzyme is further purified and concentrated, including an ultrafiltration step in which enzyme protein is retained, while most of the low molecular mass material passes the filtration membrane and is discarded.27 The applicant provided information on the identity of the substances used to control the fermentation and in the subsequent downstream processing of the food enzyme.28 ^,^ 29

The Panel considered that sufficient information has been provided on the manufacturing process and the quality assurance system implemented by the applicant to exclude issues of concern.

Characteristics of the food enzyme

3.3

Properties of the food enzyme

3.3.1

The α‐amylase is a single polypeptide chain of ■■■■■ amino acids.30 The molecular mass of the mature protein, calculated from the amino acid sequence, is ■■■■■ kDa.31 The food enzyme was analysed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis.32 A consistent protein pattern was observed across all batches. The gel showed a major protein band with a molecular mass of about ■■■■■ kDa in all batches, consistent with the expected mass of the enzyme.

No other enzyme activities were reported.

The applicant's in‐house determination of α‐amylase activity is based on the hydrolysis of starch ■■■■■. The enzyme activity is determined by measuring the decrease in starch colouration by iodine, detected spectrophotometrically ■■■■■. The enzyme activity is expressed in high‐temperature α‐amylase units (U). One U is defined as the amount of enzyme, which hydrolyses 1 mg of starch to dextrin under the conditions of the assay.33

The food enzyme has a temperature optimum around ■■■■■ and a pH optimum between ■■■■■. Thermostability was tested by pre‐incubation of the food enzyme for ■■■■■ at different temperatures. The enzyme activity decreased above 70°C and showed 65% activity at 95°C.34

Chemical parameters

3.3.2

Data on the chemical parameters of the food enzyme were provided for three batches intended for commercialisation (Table 1).35 ^,^ 36 The mean total organic solids (TOS) was 18.4% and the mean enzyme activity/TOS ratio was 80.5 U/mg TOS.

Purity

3.3.3

The lead content in the three batches was ≤ 0.017 mg/kg,37 which complies with the specification for lead, as laid down in the general specifications for enzymes used in food processing (FAO/WHO, 2006). In addition, mercury and cadmium concentrations were below the limits of quantification (LoQs) of the employed analytical methods. For arsenic, the average concentration determined in the commercial batches was 0.18 mg/kg.38 ^,^ 39 The Panel considered this concentration as not of concern.

The food enzyme preparation complies with the microbiological criteria for Enterobacteriaceae and Escherichia coli, in line with the EFSA Guidance (EFSA CEP Panel, 2021) and the general specifications for enzymes used in food processing (FAO/WHO, 2006), respectively. No antimicrobial activity was detected in any of the tested batches.40 ^,^ 41

The presence of zearalenone, deoxynivalenol and ochratoxin A was examined in three food enzyme preparation batches, and all were below the LoQs of the applied analytical methods.42 ^,^ 43 Aflatoxins, fumonisins (B1, B2 and B3) and citrinin were found in all batches tested with mean concentrations of 1.96 μg/kg, 63.7 μg/kg and > 405 μg/kg, respectively.^,^ 44

As the production strain is not able to produce these mycotoxins, the Panel considered that they could originate from contamination of the raw materials used for the fermentation. Using the highest estimated dietary exposure of 5.166 mg TOS/kg body weight (bw) per day as the reference (see Section 3.5.2), the concentration of aflatoxins and fumonisins in the food enzyme batches correspond to 0.06 and 1.8 ng/kg bw per day in regular diet of consumers, respectively. They are several orders of magnitudes lower than the safety levels derived by EFSA (EFSA CONTAM Panel, 2018, 2020). As the concentration of citrinin was not reliably quantified but reported by the applicant to exceed 405 μg/kg of food enzyme, a concern for genotoxicity and carcinogenicity could not be excluded (EFSA CONTAM Panel, 2012).

Viable cells and DNA of the production strain

3.3.4

The absence of viable cells of the production strain in the food enzyme was demonstrated in three independent batches that were analysed in triplicate. ■■■■■. No colonies were produced. A positive control was included.45

The absence of recombinant DNA in the food enzyme was demonstrated by polymerase chain reaction analysis of three batches in triplicate. No DNA was detected with primers that would amplify ■■■■■, which is smaller than the ■■■■■ gene, and therefore acceptable, with a limit of detection of 0.1 ng spiked DNA/mL food enzyme.46

Toxicological data

3.4

Although all other requirements for the QPS have been met, the production strain carries multiple copies of an acquired antimicrobial resistance gene and therefore cannot be considered as suitable for the QPS approach. However, no risk is expected from the presence of this antimicrobial resistance gene in the production strain, as the enzyme was shown not to contain viable cells or its DNA (Section 3.3.4.). As no other concerns arising from the microbial source and its subsequent genetic modification or from the manufacturing process have been identified, the Panel considered that no toxicological studies other than assessment of allergenicity are needed for the assessment of this food enzyme.

Allergenicity

3.4.1

The allergenicity assessment considered only the food enzyme and not additives, carriers or other excipients that may be used in the final formulation.

The potential allergenicity of the α‐amylase produced with the Bacillus licheniformis CCTCC M 2023118 was assessed by comparing its amino acid sequence with those of known allergens as described in the EFSA GMO Scientific Opinion (EFSA GMO Panel, 2010). Using higher than 35% identity in a sliding window of 80 amino acids as the criterion, matches with two respiratory allergens were found in the AllergenOnline and COMPARE databases.47 The matching allergens were Asp o 21 (38.7% sequence identity), an α‐amylase from Aspergillus oryzae, and an α‐amylase from Oryza sativa subsp. Japonica (52.7% sequence identity).

No reports on oral or respiratory sensitisation or elicitation reactions of the α‐amylase under assessment have been published.

α‐Amylases have been shown to cause respiratory allergy (Baur et al., 2013). Several studies have shown that individuals respiratorily sensitised to a food enzyme are usually able to ingest the corresponding enzyme without acquiring clinical symptoms of food allergy (Armentia et al., 2009; Cullinan et al., 1997; Poulsen, 2004) as also described for the α‐amylase from A. oryzae. Taking into account the wide use of α‐amylases as food enzyme, only a low number of allergic reactions upon oral exposure to α‐amylase in individuals respiratory sensitised to α‐amylase have been described in the literature (Baur & Czuppon, 1995; Kanny & Moneret‐Vautrin, 1995; Losada et al., 1992; Moreno‐Ancillo et al., 2004; Quirce et al., 1992).48

The Panel considered that the results of the sequence homology search and the available literature do not indicate a risk of allergic reactions upon dietary exposure to the α‐amylase under assessment.

■■■■■ a product from soy that may cause allergies or intolerances (listed in the Regulation (EU) No 1169/2011),49 is used as a raw material. In addition, ■■■■■, a known source of allergens, is present in the culture medium. During the fermentation process, these products will mostly be degraded and utilised by the production strain.

The Panel considered that residual amounts of allergenic proteins could be present in the food enzyme. Taking into account the level of dietary exposure (see Section 3.5.2), this would result in minute amounts in the final foods, from which allergic reactions are usually not expected.

In conclusion, when used for the production of distilled alcohols, the Panel considered that a risk of allergic reactions upon dietary exposure can be excluded. For the remaining intended uses, the risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is low.

Dietary exposure

3.5

Intended use of the food enzyme

3.5.1

The food enzyme is intended to be used in six food manufacturing processes at the recommended use levels summarised in Table 2.

TABLE 2: Intended uses and recommended use levels of the food enzyme as provided by the applicant. 50

In baking processes, the food enzyme is added to flour during the dough preparation.51 The hydrolysis by α‐amylase reduces the stiffness of the dough and improves the volume of the final product.52 The food enzyme–TOS remain in the baked foods.

In the production of cereal‐based products other than baked, the food enzyme is added to flour during dough preparation.53 The hydrolysis by the α‐amylase reduces the viscosity of the slurry, facilitating downstream processing, such as extrusion. The food enzyme–TOS remain in the cereal‐based products.

In brewing processes, the food enzyme is added to cereals before mashing.54 Together with other saccharifying enzymes, the α‐amylase converts starch to fermentable sugars.55 The food enzyme–TOS remain in the brewed products.

In the production of glucose syrups and other starch hydrolysates, the food enzyme is added during the saccharification step.56 It hydrolyses starch into dextrins and reduces viscosity. The Panel considers that the food enzyme–TOS are removed from glucose syrups and other starch hydrolysates (EFSA CEP Panel, 2023).

In distilled alcohol production, the food enzyme is added to cereals during saccharification and fermentation.57 The α‐amylase facilitates the release of fermentable sugars.58 The food enzyme–TOS are not carried over into the distilled alcohols (EFSA CEP Panel, 2023).

In the production of plant‐based analogues of milk and milk products, the food enzyme is added to the plant materials during the incubation step59 to hydrolyse the gelatinised starch and thereby to reduce viscosity.60 The food enzyme–TOS remain in the plant‐based dairy alternatives.

Based on data provided on thermostability (see Section 3.3.1) and the downstream processing steps applied in the respective food manufacturing processes, the Panel considered that the food enzyme may remain in its active form in the food manufacturing processes listed in Table 2 in which the food enzyme–TOS remain, depending on the heat treatment conditions.

Dietary exposure estimation

3.5.2

In accordance with the guidance document (EFSA CEP Panel, 2021), dietary exposure was calculated for the four food manufacturing processes where the food enzyme–TOS remain in the final foods.

Chronic exposure to the food enzyme–TOS was calculated using the FEIM webtool61 by combining the maximum recommended use level with individual consumption data (EFSA CEP Panel, 2021). The estimation involved selection of relevant food categories and application of technical conversion factors (EFSA CEP Panel, 2023).

Table 3 provides an overview of the derived exposure estimates across all surveys. Detailed mean and 95th percentile exposure to the food enzyme–TOS per age class, country and survey, as well as contribution from each FoodEx category to the total dietary exposure are reported in Appendix A – Tables 1 and 2. For the present assessment, food consumption data were available from 48 dietary surveys (covering infants, toddlers, children, adolescents, adults and the elderly), carried out in 26 European countries (Appendix B). The highest dietary exposure was estimated to be 5.166 mg TOS/kg bw per day in infants at the 95th percentile.

Uncertainty analysis

3.5.3

In accordance with the guidance provided in the EFSA opinion related to uncertainties in dietary exposure assessment (EFSA, 2006), the following sources of uncertainties have been considered and are summarised in Table 4.

The conservative approach applied to estimate the dietary exposure to the food enzyme–TOS, in particular assumptions made on the occurrence and use levels of this specific food enzyme, is likely to have led to an overestimation of the exposure.

The exclusion of two food manufacturing processes from the exposure estimation was based on > 99% of TOS removal. This is not expected to impact the overall estimate derived.

Margin of exposure

3.6

Since no toxicological assessment was considered necessary by the Panel, a margin of exposure was not calculated.

CONCLUSIONS

4

Based on the data provided on the presence of citrinin in the food enzyme preparation, the Panel could not exclude genotoxicity and carcinogenicity concerns for the α‐amylase produced with the genetically modified Bacillus licheniformis strain CCTCC M 2023118.

The production strain of the food enzyme contains multiple copies of a known antimicrobial resistance gene. However, based on the absence of viable cells and DNA from the production organism in the food enzyme, this is not considered to be a risk.

DOCUMENTATION AS PROVIDED TO EFSA

5

Application for the authorisation of alpha amylase from a genetically modified Bacillus licheniformis strain CCTCC M 2023118 as a new food enzyme. December 2024. Submitted by Sunson Industry Group Co., Ltd.

Additional information. March 2025. Submitted by Sunson Industry Group Co., Ltd.

ABBREVIATIONSAMRantimicrobial resistanceANIaverage nucleotide identitybwbody weightCASChemical Abstracts ServiceCCTCCChina Centre for Type Culture CollectionCEPEFSA Panel on Food Contact Materials, Enzymes and Processing Aids■■■■■■■■■■EINECSEuropean Inventory of Existing Commercial Chemical SubstancesFAOFood and Agricultural Organization of the United NationsFEIMFood Enzyme Intake ModelFEZEFSA Panel on Food EnzymesGMOgenetically modified organismIUBMBInternational Union of Biochemistry and Molecular BiologyJECFAJoint FAO/WHO Expert Committee on Food AdditiveskDakiloDaltonLDHlactate dehydrogenaseLoQlimit of quantificationQPSqualified presumption of safetyRMraw materialTOStotal organic solidsWGSwhole genome sequencingWHOWorld Health Organization

REQUESTOR

European Commission

QUESTION NUMBER

EFSA‐Q‐2024‐00524

COPYRIGHT FOR NON‐EFSA CONTENT

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PANEL MEMBERS

José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize de Lourdes Marzo Solano, Henk Van Loveren, Laurence Vernis and Holger Zorn.

LEGAL NOTICE

Relevant information or parts of this scientific output have been blackened in accordance with the confidentiality requests formulated by the applicant pending a decision thereon by EFSA. The full output has been shared with the European Commission, EU Member States (if applicable) and the applicant. The blackening may be subject to review once the decision on the confidentiality requests is adopted by EFSA and in case it rejects some of the confidentiality requests.

Supporting information

APPENDIX A Dietary exposure estimates to the food enzyme–TOS in details